ID   TFDE2_CUPPJ             Reviewed;         235 AA.
AC   P94136; Q46M60;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Carboxymethylenebutenolidase 2;
DE            EC=3.1.1.45;
DE   AltName: Full=Carboxymethylenebutenolidase II;
DE   AltName: Full=Dienelactone hydrolase II;
DE            Short=DLH II;
GN   Name=tfdEII; OrderedLocusNames=Reut_D6472;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OG   Plasmid pJP4, and Plasmid pPJ4.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pJP4;
RA   van der Meer J.R.;
RL   Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pJP4;
RX   PubMed=15186344; DOI=10.1111/j.1462-2920.2004.00596.x;
RA   Trefault N., De la Iglesia R., Molina A.M., Manzano M., Ledger T.,
RA   Perez-Pantoja D., Sanchez M.A., Stuardo M., Gonzalez B.;
RT   "Genetic organization of the catabolic plasmid pJP4 from Ralstonia eutropha
RT   JMP134 (pJP4) reveals mechanisms of adaptation to chloroaromatic pollutants
RT   and evolution of specialized chloroaromatic degradation pathways.";
RL   Environ. Microbiol. 6:655-668(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197; PLASMID=pPJ4;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
CC   -!- FUNCTION: Ring cleavage of cyclic ester dienelactone to produce
CC       maleylacetate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-(5-oxo-2,5-dihydrofuran-2-ylidene)acetate + H2O = 4-oxohex-
CC         2-enedioate + H(+); Xref=Rhea:RHEA:12372, ChEBI:CHEBI:12040,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57263; EC=3.1.1.45;
CC   -!- PATHWAY: Aromatic compound metabolism; 3-chlorocatechol degradation.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Carboxymethylenebutenolidase is specific for
CC       dienelactone and has no activity toward enol-lactones. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the dienelactone hydrolase family.
CC       {ECO:0000305}.
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DR   EMBL; U16782; AAC44728.1; -; Genomic_DNA.
DR   EMBL; AY365053; AAR31045.1; -; Genomic_DNA.
DR   EMBL; CP000093; AAZ65770.1; -; Genomic_DNA.
DR   RefSeq; WP_011178392.1; NZ_AY365053.1.
DR   AlphaFoldDB; P94136; -.
DR   SMR; P94136; -.
DR   ESTHER; alceu-tfe2; Dienelactone_hydrolase.
DR   EnsemblBacteria; AAZ65770; AAZ65770; Reut_D6472.
DR   KEGG; reu:Reut_D6472; -.
DR   HOGENOM; CLU_1119605_0_0_4; -.
DR   OMA; YPFPQGL; -.
DR   OrthoDB; 1756582at2; -.
DR   UniPathway; UPA00083; -.
DR   GO; GO:0008806; F:carboxymethylenebutenolidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002925; Dienelactn_hydro.
DR   Pfam; PF01738; DLH; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; Hydrolase; Plasmid; Serine esterase.
FT   CHAIN           1..235
FT                   /note="Carboxymethylenebutenolidase 2"
FT                   /id="PRO_0000161575"
FT   ACT_SITE        117
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        204
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   235 AA;  25400 MW;  3129DDA5AE48E9F3 CRC64;
     MCHDTAPALF PRTASTGSID GAICALCYAG ATRGPRLLVL PDIYGCNAFY RGYAAYLAEQ
     GAGEVLLVDP FAAFGELATV TREAAFQRRH RLADRAYVEE LIDFIDGQRI EGVVGFCLGG
     LFVFELARQQ VVSRLVAYYP FPQGLENRDP LDVPFDYLPA LRSRHTVIVG DDDALLGTQN
     LQRLQAQARA NDAIDLHIMN GAGHGFLADL ESPDTARAAV AKRGLRIGTT TLLGG